Crystallographic data collection and refinement statistics
| . | FXIIFnII-gC1qR . |
|---|---|
| Data collection | |
| Space group | I121 |
| Cell dimensions | |
| a, b, c (Å) | 106.3, 71.6, 115.9 |
| α, β, γ (°) | 90, 110.6, 90 |
| Resolution (Å) | 91.0-3.1 |
| Rmerge (%)* | 10.9 (45.5)† |
| I / σI | 7.1 (2.0)† |
| Completeness (%) | 99.9 (100.0)† |
| Redundancy | 3.1 (3.1)† |
| Wavelength (Å) | 0.97949 |
| Refinement | |
| No. of reflections | 14 378 |
| Rwork‡/Rfree (%) | 0.192/0.250 |
| No. of atoms | |
| Protein | 4752 |
| Zn2+ | 3 |
| Water | 10 |
| B-factors (Å2) | |
| Protein | 76.8 |
| Metal | 72.1 |
| Water | 46.7 |
| Root-mean-square deviations | |
| Bond lengths (Å) | 0.012 |
| Bond angles (°) | 1.57 |
| . | FXIIFnII-gC1qR . |
|---|---|
| Data collection | |
| Space group | I121 |
| Cell dimensions | |
| a, b, c (Å) | 106.3, 71.6, 115.9 |
| α, β, γ (°) | 90, 110.6, 90 |
| Resolution (Å) | 91.0-3.1 |
| Rmerge (%)* | 10.9 (45.5)† |
| I / σI | 7.1 (2.0)† |
| Completeness (%) | 99.9 (100.0)† |
| Redundancy | 3.1 (3.1)† |
| Wavelength (Å) | 0.97949 |
| Refinement | |
| No. of reflections | 14 378 |
| Rwork‡/Rfree (%) | 0.192/0.250 |
| No. of atoms | |
| Protein | 4752 |
| Zn2+ | 3 |
| Water | 10 |
| B-factors (Å2) | |
| Protein | 76.8 |
| Metal | 72.1 |
| Water | 46.7 |
| Root-mean-square deviations | |
| Bond lengths (Å) | 0.012 |
| Bond angles (°) | 1.57 |
Rmerge = sum(h) [sum(j) [I(hj) − <Ih>]/sum(hj) <Ih>, where I is the observed intensity and <Ih> is the average intensity of multiple observations from symmetry-related reflections calculated.
Values in parentheses are for highest-resolution shell.
Rwork = sum(h) ||Fo|h − |Fc|h| / sum(h)|Fo|h, where Fo and Fc are the observed and calculated structure factors, respectively. Rfree was computed as for Rwork, but only for (5%) randomly selected reflections, which were omitted in refinement, calculated using REFMAC.